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PrrC, a Sco homologue from Rhodobacter sphaeroides, possesses thiol-disulfide oxidoreductase activity
Authors:Badrick Alison C  Hamilton Amanda J  Bernhardt Paul V  Jones Christopher E  Kappler Ulrike  Jennings Michael P  McEwan Alastair G
Affiliation:Centre for Metals in Biology, School of Molecular and Microbial Sciences, The University of Queensland, Brisbane, Queensland 4072, Australia.
Abstract:PrrC is a Sco homologue in Rhodobacter sphaeroides that is associated with PrrBA, a two-component signal transduction system that induces photosynthesis gene expression in response to a decrease in oxygen tension. Although Sco proteins have been shown to bind copper the observation that they are structurally-related to thioredoxins suggested that they might possess thiol-disulfide oxidoreductase activity. Our results show that PrrC reduces Cu(2+) to Cu(+) and possesses disulfide reductase activity. These results indicate that some bacterial Sco proteins may have biochemical properties that are distinct from those of mitochondrial Sco proteins.
Keywords:BC, bathocuproine 2,9-dimethyl-4,7-diphenyl-1,10-phenanthroline   BSA, bovine serum albumin   Co(trans-diammac), trans-6,13-dimethyl-(1,4,8,11-tetraazacyclotetradecane-6,13-diamine)cobalt(III) perchlorate   cPrrC, cleaved PrrC   DTNB, 5,5-dithiobis(2-nitrobenzoic acid)   DTT, dithiothreitol, (2R,3R)-1,4-bis-sulfanylbutane-2,3-diol   EPR, Electron Paramagnetic Resonance   htPrrC, 6×-his-tagged PrrC   IPTG, isopropyl-β-  smallcaps"  >d-thiogalactopyranoside   oxPrrC, oxidised PrrC   PrrC, photosynthetic regulatory response   rPrrC, reduced PrrC   Sco, synthesis of cytochrome oxidase   Trx, thioredoxin
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